N-Terminal Sequence of Amino Acids and Some Properties of an Acid-stableα-Amylase from Citric Acid-Koji (Aspergillus usamiivar.) | Zendy

Toshihiko Suganuma | Zendy; Norihito Tahara | Zendy; Kanefumi Kitahara | Zendy; Tomonori Nagahama | Zendy; Koji Inuzuka | Zendy

Open Access

N-Terminal Sequence of Amino Acids and Some Properties of an Acid-stableα-Amylase from Citric Acid-Koji (Aspergillus usamiivar.)

Author(s) -

Toshihiko Suganuma,

Norihito Tahara,

Kanefumi Kitahara,

Tomonori Nagahama,

Koji Inuzuka

Publication year - 1996

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.60.177

Subject(s) - citric acid , aspergillus niger , chemistry , hydrolysis , amylase , enzyme , amino acid , biochemistry

An acid-stable alpha-amylase (AA) was purified from an acidic extract of citric acid-koji (A. usamii var.). The N-terminal sequence of the first 20 amino acids of the enzyme was identical with that of AA from A. niger, but the two enzymes differed in molecular weight. HPLC analysis for identifying the anomers of products indicated that the AA hydrolyzed maltopentaose (G5) at the third glycoside bond predominantly, which differed from Taka-amylase A and the neutral alpha-amylase (NA) from the citric acid-koji.

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